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ATP + H2O
ADP + phosphate
additional information
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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NTPase activity
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ATP + H2O
ADP + phosphate
EF409381
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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RNA helicase activity
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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RNA helicase activity
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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the C-terminal portion of hepatitis C virus nonstructural protein 3 (NS3) forms a three domain polypeptide that possesses the ability to travel along RNA or single-stranded DNA (ssDNA) in a 3 to 5 direction. Driven by the energy of ATP hydrolysis, this movement allows the protein to displace complementary strands of DNA or RNA
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ATP + H2O
ADP + phosphate
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multifunctional enzyme possessing serine protease, NTPase, and RNA unwinding activities
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ATP + H2O
ADP + phosphate
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NTPase activity analyzed, ambiguous helicase activity, enzyme capable for unwinding RNA and DNA
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ATP + H2O
ADP + phosphate
RNA-stimulated ATPase activities determined, interaction between the replicative component nonstructural protein 3 (NS3) with the nonstructural protein 4A (NS4A)
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ATP + H2O
ADP + phosphate
the Arg-rich amino acid motif HCV1487-1500, a fragment of domain 2 NS3 of Hepatitis C virus, as well as the complete domain 2, and domain 2 lacking the flexible loop localized between Val1458 and Thr1476, mediate competitive inhibition of diverse protein kinase C functions, inhibition of rat brain PKC, overview
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
gonadotropin-regulated testicular helicase (GRTH/DDX25), a target of gonadotropin and androgen action, is a post-transcriptional regulator of key spermatogenesis genes. GRTH has a negative role on its mRNA stability
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ATP + H2O
ADP + phosphate
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RHA is a coactivator in STAT6-mediated transcription, and this function is dependent on its helicase activity
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ATP + H2O
ADP + phosphate
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation
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ATP + H2O
ADP + phosphate
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation. DDX17 is involved in mRNA splicing
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ATP + H2O
ADP + phosphate
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translation of HIV-1 gag mRNA is reliant on the ATP-dependent helicase activity of RNA helicase A
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation
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ATP + H2O
ADP + phosphate
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation. DDX17 is involved in mRNA splicing
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation. DDX17 is involved in mRNA splicing
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
Mtr4p can unwind duplex RNA in the presence of ATP and a single-stranded RNA tail in the 3' to 5' direction
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ATP + H2O
ADP + phosphate
the DEAD-box protein DED1 has the ability to balance RNA unwinding with a profound strand annealing activity in a highly dynamic fashion
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
Thermochaetoides thermophila
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ATP + H2O
ADP + phosphate
Thermochaetoides thermophila
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ATP + H2O
ADP + phosphate
Thermochaetoides thermophila CBS 144.50
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ATP + H2O
ADP + phosphate
Thermochaetoides thermophila CBS 144.50
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ATP + H2O
ADP + phosphate
Thermochaetoides thermophila DSM 1495
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ATP + H2O
ADP + phosphate
Thermochaetoides thermophila DSM 1495
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ATP + H2O
ADP + phosphate
Thermochaetoides thermophila IMI 039719
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ATP + H2O
ADP + phosphate
Thermochaetoides thermophila IMI 039719
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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phosphohydrolase and helicase activities of NPH-II are essential for virus replication
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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the West Nile virus RNA helicase uses the energy derived from the hydrolysis of nucleotides to separate complementary strands of RNA
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ATP + H2O
ADP + phosphate
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RNA + H2O
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RNA unwinding activity, the enzyme contains two RecA-like domains, opening and closing of the interdomain cleft during RNA unwinding
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RNA + H2O
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EF409381
helicase/unwinding activity, either ATP or dATP is required for the unwinding activity
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RNA + H2O
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helicase/unwinding activity
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using yeast two-hybrid and pull-down assays it is shown that RH22 interacts with the 50S ribosomal protein RPL24
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ISE2 associates with numerous chloroplast RNA species, chloroplast rRNAs are potential ISE2 substrates. ISE2 associates with transcripts containing C-to-U editing sites
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ISE2 associates with numerous chloroplast RNA species, chloroplast rRNAs are potential ISE2 substrates. ISE2 associates with transcripts containing C-to-U editing sites
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additional information
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ISE2 associates with numerous chloroplast RNA species, chloroplast rRNAs are potential ISE2 substrates. ISE2 associates with transcripts containing C-to-U editing sites
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BMV 1a protein accumulates on endoplasmic reticulum membranes of the host cell, recruits the other RNA replication factor 2apol and induces 50- to 70-nm membrane invaginations serving as RNA replication compartments, BMV 1a protein also recruits viral replication templates such as genomic RNA3 depending on the BMV 1a protein helicase motif, in absence of 2apol, BMV 1a protein highly stabilizes RNA3 by transferring it to a membrane-associated, nuclease-resistant state, overview
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DEAD box proteins are putative RNA unwinding proteins, BmL3-helicase also is a DEAD box RNA helicase
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EF409381
DEAD box proteins are putative RNA unwinding proteins, BmL3-helicase also is a DEAD box RNA helicase
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NS3 possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. Functions of NS3 and NS5B during positive-strand RNA virus replication, the NS3 protein is be involved in the unwinding of the viral RNA template while NS5B protein may be involved in catalyzing the synthesis of new RNA molecules
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additional information
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NS3 possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. Functions of NS3 and NS5B during positive-strand RNA virus replication, the NS3 protein is be involved in the unwinding of the viral RNA template while NS5B protein may be involved in catalyzing the synthesis of new RNA molecules
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additional information
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NS3 possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. Functions of NS3 and NS5B during positive-strand RNA virus replication, the NS3 protein is be involved in the unwinding of the viral RNA template while NS5B protein may be involved in catalyzing the synthesis of new RNA molecules
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the enzyme plays an important role in viral replication
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The NS3 protein physically associates with the NS5 polymerase, NS3 andNS5 carry out all the enzymatic activities needed for polyprotein processing and genome replication. NS3 possesses an ATPase/helicase and RNA triphosphatase at its C-terminal end that are essential for RNA replication. In addition to its known enzymatic functions, the NS3 protein appears to be involved in the assembly of an infectious flaviviral particle, through its interactions with NS2A and presumably host cell proteins
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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nonstructural proteins NS3 and NS5 form complexes in infected mammalian cells
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helicase B, RhlB, is one of the five DEAD box RNA-dependent ATPases in Escherichia coli. ATPases found in Escherichia coli. RhlB requires an interaction with the partner protein RNase E for appreciable ATPase and RNA unwinding activities
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the enzyme is involved in viral replication
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additional information
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the C-terminal region of NS3 exhibits RNA-stimulated NTPase, e.g. ATPase, and helicase activity, while the N-terminal serine protease domain of NS3 enhances RNA binding and unwinding by the C-terminal region, NS4A mutants that are defective in ATP-coupled RNA binding are lethal in vivo
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additional information
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the C-terminal region of NS3 exhibits RNA-stimulated NTPase, e.g. ATPase, and helicase activity, while the N-terminal serine protease domain of NS3 enhances RNA binding and unwinding by the C-terminal region, NS4A mutants that are defective in ATP-coupled RNA binding are lethal in vivo
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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DEAD-Box RNA Helicase DDX3 interacts with DDX5. The protein-protein interaction is increased in the G2/M phase
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DEAD-Box RNA Helicase DDX3 interacts with DDX5. The protein-protein interaction is increased in the G2/M phase
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human telomerase RNA interacts with the N-terminal domain of RHAU
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p68 interacts with an intronic splicing activator, RNA binding motif protein 4 (RBM4), thereby stimulating tau exon 10 inclusion
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recombinant N-terminal, central helicase, and C-terminal domains of RHA are evaluated for their ability to specifically interact with cognate RNAs by in vitro biochemical measurements and mRNA translation assays in cells. Results demonstrate that N-terminal residues confer selective interaction with retroviral and junD target RNAs. Conserved lysine residues in the distal alpha-helix of the double-stranded RNA-binding domains are necessary to engage structural features of retroviral and junD 5'-UTRs
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RNA helicase A interacts with La ribonucleoprotein domain family member 6 (LARP6) which recruits RHA to the 5' UTR of collagen mRNAs
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ChlR1 robustly unwinds DNA triplex substrates in an ATP-dependent manner requiring an 5'-ssDNA tail, ChlR1 can unwind an intramolecular triplex structure
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ChlR1 robustly unwinds DNA triplex substrates in an ATP-dependent manner requiring an 5'-ssDNA tail, ChlR1 can unwind an intramolecular triplex structure
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enzyme DDX21 inhibits influenza A virus replication. Enzyme DDX21 most likely binds viral PB1 protein in the cytoplasm, where protein PB1 is probably free of the other polymerase subunits, albeit transiently, before it forms a complex with viral protein PA that is imported into the nucleus
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human Upf1 is able to translocate slowly over long single-stranded nucleic acids with a high processivity. Upf1 efficiently translocates through double-stranded structures and protein-bound sequences. The helicase domain of Upf1 is capable of both unwinding double-stranded nucleic acids and translocation on single-stranded nucleic acids over long distances. Upf1 remodels nucleoprotein complexes
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human Upf1 is able to translocate slowly over long single-stranded nucleic acids with a high processivity. Upf1 efficiently translocates through double-stranded structures and protein-bound sequences. The helicase domain of Upf1 is capable of both unwinding double-stranded nucleic acids and translocation on single-stranded nucleic acids over long distances. Upf1 remodels nucleoprotein complexes
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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wild-type and mutant enzymes in vitro RNA binding and unwinding or in the cell during HIV-1 production during RNA helicase A-RNA interaction and RNA helicase A-stimulated viral RNA processes, overview
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enzyme Brr2 catalyzes an ATP-dependent unwinding of the U4/U6 RNA duplex
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multiple cross-links between Aquarius and hSyf1, hIsy1, CCDC16 or CypE, with the majority of the cross-linked residues located in domains or structural insertions specific for Aquarius, such as the ARM, pointer and thumb domains, and in the large insertions of the beta-barrel
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additional information
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multiple cross-links between Aquarius and hSyf1, hIsy1, CCDC16 or CypE, with the majority of the cross-linked residues located in domains or structural insertions specific for Aquarius, such as the ARM, pointer and thumb domains, and in the large insertions of the beta-barrel
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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helicase DDX6 colocalizes with TRIM32 in neural stem cells and neurons and increases the activity of Let-7a. The activation of Let-7a depends on the enzyme's helicase activity
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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the NS3 protein of Rice hoja blanca virus is an RNA silencing suppressor, RSS, that exclusively binds to small dsRNA molecules. This plant viral RSS lacks interferon antagonistic activity, yet it is able to substitute the RSS function of the Tat protein of Human immunodeficiency virus type 1 based on the sequestration of small dsRNA. NS3 is able to inhibit endogenous miRNA action in mammalian cells
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additional information
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the NS3 protein of Rice hoja blanca virus is an RNA silencing suppressor, RSS, that exclusively binds to small dsRNA molecules. This plant viral RSS lacks interferon antagonistic activity, yet it is able to substitute the RSS function of the Tat protein of Human immunodeficiency virus type 1 based on the sequestration of small dsRNA. NS3 is able to inhibit endogenous miRNA action in mammalian cells
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additional information
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the NS3 protein of Rice hoja blanca virus is an RNA silencing suppressor, RSS, that exclusively binds to small dsRNA molecules. This plant viral RSS lacks interferon antagonistic activity, yet it is able to substitute the RSS function of the Tat protein of Human immunodeficiency virus type 1 based on the sequestration of small dsRNA. NS3 is able to inhibit endogenous miRNA action in mammalian cells
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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TaRH1-catalysed unwinding of duplex RNA
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additional information
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NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain presumably involved in viral replication
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additional information
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NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain presumably involved in viral replication
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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